Fructose 2,6‐Bisphosphate

Schaftingen, Emile Van

doi:10.1002/9780470123058.ch7

Cited by 171 publications

(65 citation statements)

References 360 publications

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“…The effects of AMPK on glucose metabolism in the heart are accounted for by the enhanced translocation of glucose transport proteins to the sarcolemma (14,43) and by the stimulation of glycolysis through the phosphorylation and activation of 6-phosphofructo-2-kinase (PFK-2) (36). The consequent increase in fructose-2,6-diphosphate (F-2,6-P 2 ) leads to the allosteric activation of PFK-1, a major determinant of glycolytic rates in the heart and other tissues (36,53).…”

mentioning

confidence: 99%

AMP-activated protein kinase influences metabolic remodeling in H9c2 cells hypertrophied by arginine vasopressin

Saeedi

Saran²,

Wu³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

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Substrate use switches from fatty acids toward glucose in pressure overload-induced cardiac hypertrophy with an acceleration of glycolysis being characteristic. The activation of AMP-activated protein kinase (AMPK) observed in hypertrophied hearts provides one potential mechanism for the acceleration of glycolysis. Here, we directly tested the hypothesis that AMPK causes the acceleration of glycolysis in hypertrophied heart muscle cells. The H9c2 cell line, derived from the embryonic rat heart, was treated with arginine vasopressin (AVP; 1 M) to induce a cellular model of hypertrophy. Rates of glycolysis and oxidation of glucose and palmitate were measured in nonhypertrophied and hypertrophied H9c2 cells, and the effects of inhibition of AMPK were determined. AMPK activity was inhibited by 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo-[1,5-a]pyrimidine (compound C) or by adenovirus-mediated transfer of dominant negative AMPK. Compared with nonhypertrophied cells, glycolysis was accelerated and palmitate oxidation was reduced with no significant alteration in glucose oxidation in hypertrophied cells, a metabolic profile similar to that of intact hypertrophied hearts. Inhibition of AMPK resulted in the partial reduction of glycolysis in AVP-treated hypertrophied H9c2 cells. Acute exposure of H9c2 cells to AVP also activated AMPK and accelerated glycolysis. These elevated rates of glycolysis were not altered by AMPK inhibition but were blocked by agents that interfere with Ca 2ϩ signaling, including extracellular EGTA, dantrolene, and 2-aminoethoxydiphenyl borate. We conclude that the acceleration of glycolysis in AVP-treated hypertrophied heart muscle cells is partially dependent on AMPK, whereas the acute glycolytic effects of AVP are AMPK independent and at least partially Ca 2ϩ dependent. cardiac hypertrophy; energy metabolism; glucose utilization

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mentioning

confidence: 99%

AMP-activated protein kinase influences metabolic remodeling in H9c2 cells hypertrophied by arginine vasopressin

Saeedi

Saran²,

Wu³

et al. 2009

American Journal of Physiology-Heart and Circulatory Physiology

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“…Dong Ji, Zhong-Tang Lu, Yao-Qing Li, Zhe-Yong Liang, Peng-Fei Zhang, Chao Li, Jun-Li Zhang, Xin Zheng, Ying-Min Yao* et al, 2013), especially on the regulation of the key enzyme in glycolysis, 6-phosphoric acid fructose kinase-1 (PFK-1) is the most important enzyme on regulation sugar flow and energy supply in glycolysis pathway, and its active height was often affect by a potent allosteric agent-fructose 2, 6-bisphosphate, which was produced by a bifunctional enzyme 6-phosphofructo-2-kinase/fructose 2, 6 bisphosphatase (PFK-2/FBPase-2) (Van Schaftingen, 1987;Okar et al, 2001;Rider et al, 2004). PFKFB2 is one of isoenzymes of PFK-2/FBase-2.And recent study found that the activation of Akt contribute to enhance the PPFKFB2's function (Moon et al, 2011;Novellasdemunt et al, 2013).…”

Section: Macc1 Expression Correlates With Pfkfb2 and Survival In Hepamentioning

confidence: 99%

MACC1 Expression Correlates with PFKFB2 and Survival in Hepatocellular Carcinoma

Lu²,

Li³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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“…Synthesis and degradation of fructose-2,6-bisphosphate: -Kinase catalytic activity: ATP + D-fructose-6-phosphate = ADP + beta-D-fructose-2,6-bisphosphate -Phosphatase catalytic activity: Beta-D-fructose-2,6-bisphosphate + H 2 O = D-fructose-6-phosphate + phosphate The rate of glycolytic flux is controlled at different levels and by different mechanisms: substrate availability, enzyme concentrations, allosteric effectors and covalent modification on regulatory enzymes. One of the critically modulated steps is that catalysed by 6-phosphofructo-1-kinase (PFK-1), with fructose-2,6-bisphosphate (Fru-2,6-P2) being its most powerful allosteric activator (Okar and Lange, 1999;Rider et al, 2004;Van Schaftingen, 1987). Fru-2,6-P2 relieves ATP inhibition and acts synergistically with AMP, and in addition it inhibits fructose 1,6-bisphosphatase (Van Schaftingen, 1987).…”

Section: Functionmentioning

confidence: 99%

“…One of the critically modulated steps is that catalysed by 6-phosphofructo-1-kinase (PFK-1), with fructose-2,6-bisphosphate (Fru-2,6-P2) being its most powerful allosteric activator (Okar and Lange, 1999;Rider et al, 2004;Van Schaftingen, 1987). Fru-2,6-P2 relieves ATP inhibition and acts synergistically with AMP, and in addition it inhibits fructose 1,6-bisphosphatase (Van Schaftingen, 1987). These properties confer to this metabolite a key role in the control of fructose-6-P/fructose-1,6-P2 substrate cycle and hence critically regulate carbohydrate metabolism (Figure 4).…”

Section: Functionmentioning

confidence: 99%